First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1vec
From Proteopedia
| 1vec, resolution 2.01Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||||
| Ligands: | , | ||||||||
| Gene: | HUMRCK (Homo sapiens) | ||||||||
| Domains: | DEADc | ||||||||
| Related: | 1qde, 1qva, 1q0u | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of the N-terminal domain of rck/p54, a human DEAD-box protein
Human rck/p54, a product of the gene cloned at the breakpoint of t(11; 14) (q23;q32) chromosomal translocation on 11q23 in B-cell lymphoma, is a member of the DEAD-box RNA helicase family. Here, the crystal structure of Nc-rck/p54, the N-terminal core domain of rck/p54, revealed that the P-loop in motif I formed a closed conformation, which was induced by Asn131, a residue unique to the RCK subfamily. It appears that ATP does not bind to the P-loop. The results of dynamic light scattering revealed to ATP-induced conformational change of rck/p54. It was demonstrated that free rck/p54 is a distended molecule in solution, and that the approach between N-terminal core and C-terminal domains for ATP binding would be essential when unwinding RNA. The results from helicase assay using electron micrograph, ATP hydrolytic and luciferase assay showed that c-myc IRES RNA, whose secondary structure regulates IRES-dependant translation, was unwound by rck/p54 and indicated that it is a good substrate for rck/p54. Over-expression of rck/p54 in HeLa cells caused growth inhibition and cell cycle arrest at G2/M with down-regulation of c-myc expression. These findings altogether suggest that rck/p54 may affect the IRES-dependent translation of c-myc even in the cells.
Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes., Matsui T, Hogetsu K, Usukura J, Sato T, Kumasaka T, Akao Y, Tanaka N, Genes Cells. 2006 Apr;11(4):439-52. PMID:16611246
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1VEC is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Matsui T, Hogetsu K, Usukura J, Sato T, Kumasaka T, Akao Y, Tanaka N. Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes. Genes Cells. 2006 Apr;11(4):439-52. PMID:16611246 doi:10.1111/j.1365-2443.2006.00951.x
Page seeded by OCA on Mon Feb 16 20:15:57 2009

